ID   PFDA_NATPD              Reviewed;         151 AA.
AC   Q3IUJ7;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Prefoldin subunit alpha {ECO:0000255|HAMAP-Rule:MF_00308};
DE   AltName: Full=GimC subunit alpha {ECO:0000255|HAMAP-Rule:MF_00308};
GN   Name=pfdA {ECO:0000255|HAMAP-Rule:MF_00308}; OrderedLocusNames=NP_0184A;
OS   Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS   8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Natronomonas.
OX   NCBI_TaxID=348780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC   2260 / Gabara;
RX   PubMed=16169924; DOI=10.1101/gr.3952905;
RA   Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA   Oesterhelt D.;
RT   "Living with two extremes: conclusions from the genome sequence of
RT   Natronomonas pharaonis.";
RL   Genome Res. 15:1336-1343(2005).
CC   -!- FUNCTION: Molecular chaperone capable of stabilizing a range of
CC       proteins. Seems to fulfill an ATP-independent, HSP70-like function in
CC       archaeal de novo protein folding. {ECO:0000255|HAMAP-Rule:MF_00308}.
CC   -!- SUBUNIT: Heterohexamer of two alpha and four beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00308}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00308}.
CC   -!- SIMILARITY: Belongs to the prefoldin subunit alpha family.
CC       {ECO:0000305}.
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DR   EMBL; CR936257; CAI48183.1; -; Genomic_DNA.
DR   RefSeq; WP_011321822.1; NC_007426.1.
DR   AlphaFoldDB; Q3IUJ7; -.
DR   SMR; Q3IUJ7; -.
DR   STRING; 348780.NP_0184A; -.
DR   EnsemblBacteria; CAI48183; CAI48183; NP_0184A.
DR   GeneID; 3703017; -.
DR   KEGG; nph:NP_0184A; -.
DR   eggNOG; arCOG01341; Archaea.
DR   HOGENOM; CLU_091867_1_3_2; -.
DR   OMA; ELQNQFM; -.
DR   OrthoDB; 105878at2157; -.
DR   Proteomes; UP000002698; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016272; C:prefoldin complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.287.370; -; 1.
DR   HAMAP; MF_00308; PfdA; 1.
DR   InterPro; IPR011599; PFD_alpha_archaea.
DR   InterPro; IPR009053; Prefoldin.
DR   InterPro; IPR004127; Prefoldin_subunit_alpha.
DR   PANTHER; PTHR12674; PTHR12674; 1.
DR   Pfam; PF02996; Prefoldin; 1.
DR   TIGRFAMs; TIGR00293; TIGR00293; 1.
PE   3: Inferred from homology;
KW   Chaperone; Cytoplasm; Reference proteome.
FT   CHAIN           1..151
FT                   /note="Prefoldin subunit alpha"
FT                   /id="PRO_0000300768"
FT   REGION          120..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   151 AA;  16555 MW;  ACDD4C27D1977626 CRC64;
     MSLGGGGGGG AMEQIQQQLQ ALEQEKQAIQ AEIENVRDEQ SEIDEAIEAI ETLETGATVQ
     VPLGGDAYVR ATIEDMDEVV VTLGGGYAAE RDSEGAVESL ERKKETLDDR IEELEGEIET
     VEEETASLEE KAQQAQQQQM QQLQQMQQED E